ELFT: A gene that directs the expression of an ELAM-1 ligand

Goelz, Susan; Hession, Catherine; Goff, Deborah J.; Griffiths, Beth; Tizard, Richard; Newman, Barbara M.; Chi-Rosso, G; Lobb, Roy R.

doi:10.1016/0092-8674(90)90430-m

Cited by 318 publications

(154 citation statements)

References 33 publications

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“…These results corroborated our previous conclusion that FUT3 was the enzyme involved in the synthesis of Le a , sLe a and Le b in GG cells. FUT4 was detected at 59 kDa that probably corresponded to the long form ELFT-L (predicted molecular mass 59 kDa) identified by Goelz et al (37). FUT9 whose predicted molecular mass from the amino acid sequence is 42 kDa, appeared at 46 kDa.…”

Section: Detection Of Fut3 Fut4 Fut5 and Fut9 In Ovarian Carcinoma mentioning

confidence: 68%

Different expression levels of α3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines

Escrevente

Machado²,

Brito³

et al. 2006

Int J Oncol

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Section: Detection Of Fut3 Fut4 Fut5 and Fut9 In Ovarian Carcinoma mentioning

confidence: 68%

Different expression levels of α3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines

Escrevente

Machado²,

Brito³

et al. 2006

Int J Oncol

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“…Human Fuc-TIV, also termed ELFT for ELAM-1 ligand fucosyltransferase, was reported to generate E-selectin binding carbohydrate modifications (8). However, this activity has been observed only when the enzyme is expressed at a certain level and in cells with a certain glycosylation phenotype (9 -13).…”

mentioning

confidence: 99%

The α(1,3)-Fucosyltransferase Fuc-TIV, but Not Fuc-TVII, Generates Sialyl Lewis X-like Epitopes Preferentially on Glycolipids

Huang

Laskowska²,

Vestweber

et al. 2002

Journal of Biological Chemistry

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Fuc-TIV and Fuc-TVII are the two ␣(1, 3)-fucosyltransferases in myeloid cells responsible for the biosynthesis of sialyl Lewis X (sLe x ), the minimal ligand structure for the selectins. We have compared the ability of Fuc-TIV and Fuc-TVII to generate sLe x -like epitopes in transfected Chinese hamster ovary (CHO)-Pro ؊ 5 cells expressing the P-selectin glycoprotein ligand-1 and the core-2 branching enzyme C2GnT. We found that mouse Fuc-TIV and Fuc-TVII can generate similar levels of cell surface sLe x . Surprisingly however, Fuc-TIV-generated sLe x was resistant to proteinase K and trypsin treatment and could be removed from cells by delipidation with chloroform/methanol, whereas 80 -90% of Fuc-TVIIgenerated sLe x was protease-sensitive, and most of it resistant to delipidation. Despite similar levels of sLe x on the cell surface, Fuc-TVII transfectants adhered to immobilized E-selectin-IgG under static and flow conditions better than Fuc-TIV transfectants. Binding was mainly protease sensitive, indicating that glycoproteins were more efficient ligands than glycolipids. In summary, we conclude that the two fucosyltransferases differ in their in vivo specificity for acceptor substrates with Fuc-TVII generating sLe x preferentially on glycoproteins, whereas most of the Fuc-TIV-generated sLe x is found on glycolipids. Interestingly, the non-catalytic portion of Fuc-TIV in a Fuc-TIV/VII chimeric enzyme mediated the specificity for glycolipid substrates.The three known selectins, L-, E-, and P-selectin are cell adhesion molecules that initiate interactions between leukocytes and endothelial cells during leukocyte extravasation (1). The minimal ligand structure for all three selectins is the tetrasaccharide sialyl Lewis X (sLe x ). 1

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“…At baseline FucT-IV/FucT-VII-deficient mice showed a large number of renal neutrophils. This is due to the inherent defect in leukocyte extravasation from the circulation and neutrophilia in these mice (16). Despite increased numbers at baseline, relative increases in PMN counts postischemia were significantly decreased in FucT-IV/FucT-VII-deficient mice compared with wild-type mice.…”

Section: Discussionmentioning

confidence: 93%

“…Two mammalian FucT loci, termed FucT-IV and FucT-VII, have been implicated in the control of leukocyte selectin ligand activities by virtue of their expression patterns, the structure of the fucosylated glycans they elaborate, and analysis of mice with induced null mutations in these loci (13)(14)(15). FucT-IV was the first leukocyte-associated enzyme linked to selectin-ligand synthesis (16,17). FucT-IV, can synthesize the Le x , Le y , and sLe x epitopes, although the activity for sLe x synthesis is very weak.…”

mentioning

confidence: 99%

Pathophysiological Contributions of Fucosyltransferases in Renal Ischemia Reperfusion Injury

Burne

Rabb

2002

The Journal of Immunology

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Ischemia reperfusion injury (IRI) is a major cause of delayed graft function. Recent studies have shown that selectins play an important role in IRI. Selectins bind to sialylated and fucosylated sLex receptors, and two enzymes, fucosyltransferase IV (FucT-IV) and VII (FucT-VII), are important in the function of these receptors. We hypothesized that fucosyltransferase (FucT) enzymes were important pathophysiologic mediators of renal IRI. We therefore evaluated renal IRI in mice deficient in FucT-IV, FucT-VII, and both FucT-IV and FucT-VII and compared their renal function, tubular injury, selectin ligand expression, and neutrophil infiltration to those in wild-type control mice. Bilateral 30-min renal IRI was performed, and the results demonstrated that mice deficient in both FucT-IV/FucT-VII were significantly protected from renal IRI at 24 and 48 h compared with wild-type control mice. FucT-IV-deficient mice showed only modest protection from renal injury at 24 h. However, FucT-VII-deficient mice had similar injury as wild-type mice. Histological analysis of kidney tissue postischemia revealed that mice deficient in both FucT-IV and FucT-VII had significantly reduced tubular injury compared with wild-type mice. Selectin ligand expression increased postischemia in wild-type, but not FucT-IV/FucT-VII-deficient, mice. Neutrophil infiltration in postischemic kidneys of FucT-IV/FucT-VII-deficient mice was also attenuated. These data demonstrate that fucosyltransferases are important in the pathogenesis of renal IRI and are potential therapeutic targets.

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ELFT: A gene that directs the expression of an ELAM-1 ligand

Cited by 318 publications

References 33 publications

Different expression levels of α3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines

Different expression levels of α3/4 fucosyltransferases and Lewis determinants in ovarian carcinoma tissues and cell lines

The α(1,3)-Fucosyltransferase Fuc-TIV, but Not Fuc-TVII, Generates Sialyl Lewis X-like Epitopes Preferentially on Glycolipids

Pathophysiological Contributions of Fucosyltransferases in Renal Ischemia Reperfusion Injury

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